Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia
- PMID: 1586590
- PMCID: PMC1977372
- DOI: 10.1038/bjc.1992.138
Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia
Abstract
A sequential, quantitative loss of Peanut agglutinin (PNA) binding with progression of mouse mammary cells from normal to preneoplastic to neoplastic phenotypes was observed. Normal mammary epithelium, preneoplastic mammary lesions designated D2HAN (D2-type hyperplastic alveolar nodules) and a series of nine spontaneous tumours (D2ST1, D2ST2, D2ST3, D2ST4, D2A1, D2F2, D2.0R, D2.1, EMT6R08) derived from mice bearing D2HAN were grown in culture and analysed by flow cytometry with respect to PNA binding intensity to the cell surface. Primary cultures of normal mammary epithelium strongly bound PNA. A stepwise decrease in PNA binding by preneoplastic D2HAN cells and subsequent tumours arising from those hyperplastic lesions was observed. Three cloned tumour subpopulations derived from such tumours exhibited dramatic differences in PNA binding ranging from high (D2.0R) to low (D2.1) to very low (D2A1 cells). Their growth rate in vitro was similar. However, an inverse correlation between PNA binding and malignant characteristics, such as the incidence and latency of subcutaneous tumours and the efficiency of the tumour cells to form lung colonies after i.v. injection, existed. Cells subsequently derived from tumours resulting from injection of the D2.0R clone (high PNA binding, low tumorigenicity) were found to have diminished PNA binding properties and to be more tumorigenic when reimplanted into syngeneic mice. The difference in PNA binding (up to 50-fold) between normal mammary cells and other mouse mammary tumour cells, i.e., unrelated to D2HAN lesions, was also seen. These include six sister subpopulations derived from a single BALB/cfC3H mouse mammary tumour (lines: 67, 66c14, 168FARN, 4TO7, 68H, 64pT) as well as SP1 spontaneous CBA/J mouse mammary carcinoma. The difference was greatly reduced by neuraminidase treatment suggesting a masking of PNA binding sites by sialic acid. Separation of cell lysates by SDS-PAGE revealed a high molecular weight PNA binding glycoprotein (greater than 250 kd) expressed by normal mammary epithelium and preneoplastic D2HAN cells, but not by tumour cells regardless of neuraminidase treatment. A PNA reactive glycoprotein of approximately 90 kd was uniquely expressed in normal mammary epithelial lysates, although neuraminidase treatment exposed a similar band in a few tumour lines. Normal mammary epithelium, preneoplastic D2HAN cells, and the poorly tumorigenic clone D2.0R expressed a PNA binding glycoprotein of approximately 150 kd. This band appeared to be specifically sialylated during transition from the high PNA binding, low tumorigenic phenotype of D2.0R cells to the low PNA binding, highly tumorigenic phenotype of cells isolated from tumours resulting from s.c. implantation of D2.0R cells.(ABSTRACT TRUNCATED AT 400 WORDS)
Similar articles
-
Cell line specific abnormalities in expression of PNA, SBA and L-PHA binding sites by carcinogen induced rat urothelial carcinomas.Neoplasma. 1992;39(3):141-6. Neoplasma. 1992. PMID: 1528317
-
Tumor progression and metastasis in murine D2 hyperplastic alveolar nodule mammary tumor cell lines.Clin Exp Metastasis. 1993 Jan;11(1):103-12. doi: 10.1007/BF00880071. Clin Exp Metastasis. 1993. PMID: 8422701
-
Cell surface glycoproteins of 13762NF mammary adenocarcinoma clones of differing metastatic potentials.Exp Cell Res. 1983 Sep;147(2):255-67. doi: 10.1016/0014-4827(83)90208-2. Exp Cell Res. 1983. PMID: 6688589
-
Hormonal induction of mammary tumor viruses and its implications for carcinogenesis.Cancer Res. 1978 Nov;38(11 Pt 2):4112-25. Cancer Res. 1978. PMID: 212187 Review.
-
Genetic manipulation of mammary epithelium by transplantation.J Mammary Gland Biol Neoplasia. 1996 Jan;1(1):75-89. doi: 10.1007/BF02096304. J Mammary Gland Biol Neoplasia. 1996. PMID: 10887482 Review.
Cited by
-
Breast Cancer Metastatic Dormancy and Relapse: An Enigma of Microenvironment(s).Cancer Res. 2022 Dec 16;82(24):4497-4510. doi: 10.1158/0008-5472.CAN-22-1902. Cancer Res. 2022. PMID: 36214624 Free PMC article. Review.
-
Live Cell Lineage Tracing of Dormant Cancer Cells.Adv Healthc Mater. 2023 Jun;12(14):e2202275. doi: 10.1002/adhm.202202275. Epub 2023 Jan 20. Adv Healthc Mater. 2023. PMID: 36625629 Free PMC article.
-
FGFR1 Signaling Facilitates Obesity-Driven Pulmonary Outgrowth in Metastatic Breast Cancer.Mol Cancer Res. 2024 Mar 1;22(3):254-267. doi: 10.1158/1541-7786.MCR-23-0955. Mol Cancer Res. 2024. PMID: 38153436 Free PMC article.
-
Syndecan-Mediated Ligation of ECM Proteins Triggers Proliferative Arrest of Disseminated Tumor Cells.Cancer Res. 2019 Dec 1;79(23):5944-5957. doi: 10.1158/0008-5472.CAN-19-1165. Epub 2019 Sep 3. Cancer Res. 2019. PMID: 31481497 Free PMC article.
-
Integrin beta1-focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs.Proc Natl Acad Sci U S A. 2009 Jun 23;106(25):10290-5. doi: 10.1073/pnas.0904227106. Epub 2009 Jun 5. Proc Natl Acad Sci U S A. 2009. PMID: 19502425 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Research Materials